Composition and structure of zinc-deficient Euglena gracilis chromatin

Abstract

The histone content of zinc-deficient (-Zn) Euglena gracilis decreases while, concomitantly, DNA content increases and the transcription rate is reduced markedly [Mazus, B., Falchuk, K. H., & Vallee, B. L. (1983) Biochemistry (in press); Falchuk, K. H., Fawcett, D. W., & Vallee, B. L. (1975) J. Cell Sci. 17, 57-78]. The effects on major constituents of the genome have been examined by studying the rate and extent of hydrolysis of +Zn and -Zn chromatin by micrococcal nuclease, DNase I, or DNase II. The size of hydrolyzed DNA fragments suggests similarity of the +Zn E. gracilis chromatin organization to that of other eukaryotes. The major protein constituent of -Zn chromatin is a polypeptide of less than 3000 daltons whose electrophoretic mobility differs from that of any known histone components of chromatin, the latter described elsewhere (K. H. Falchuk et al., unpublished results). This protein profoundly affects the structure of -Zn chromatin, which is about 10-30-fold more resistant to micrococcal nuclease hydrolysis than +Zn chromatin. Moreover, the resultant DNA fragments [2000 base pairs (bp)], are much larger than those of +Zn cells. Under conditions which hydrolyze +Zn chromatin into DNA fragments smaller than 50 bp, only 50% of -Zn chromatin is digested into fragments less than 2000 bp, i.e., in the range of those expected for oligonucleosomes. Removal of the low molecular weight protein from -Zn chromatin reverses its enhanced resistance to nucleolysis and results in extensive hydrolysis. Conversely, addition of the low molecular weight protein to +Zn chromatin increases the resistance of this complex to digestion.(ABSTRACT TRUNCATED AT 250 WORDS)